A role of VLA‐6 laminin receptor in invasion of breast carcinoma

Arihiro, Koji; Inai, Kei; Kurihara, Kanji; Takeda, Shinpei; Khatun, Nasima; Kuroi, Katsumasa; Toge, Tetsuya

doi:10.1111/j.1440-1827.1993.tb02550.x

Cited by 6 publications

(5 citation statements)

References 26 publications

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“…Our finding that an anti-VLA-4 mAb inhibited migration of the transfectants on laminin to which VLA-4 is not known to bind was unexpected. Although VLA-4 is recognized to play a major role in the migratory activity of several cells, VLA-6 has been not been linked to cell motility, but rather to the regulation of differentiated events (35,36). However, a recent report that an anti-VLA-6 mAb could partially inhibit pre-B cell transmigration under human bone marrow stroma suggests that VLA-6 may also function in cooperation with other adhesion molecules to modulate motile behavior (37).…”

Section: Cd9 Enhanced Motility and Tyrosine Phosphorylationmentioning

confidence: 99%

Ectopic Expression of Human and Feline CD9 in a Human B Cell Line Confers β1 Integrin-dependent Motility on Fibronectin and Laminin Substrates and Enhanced Tyrosine Phosphorylation

Shaw

Domanska

Mak

et al. 1995

Journal of Biological Chemistry

124

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Few molecules have been shown to confer cell motility. Although the motility-arresting properties of anti-CD9 monoclonal antibody (mAb) suggest the transmembrane 4 superfamily (TM4SF) member CD9 can induce a motorgenic signal, gene transfection studies have failed to confirm this hypothesis. We report here that ectopic expression of human CD9 (CD9h) and feline CD9 (CD9f) in the CD9-negative, poorly motile, human B cell line Raji dramatically enhances migration across fibronectin-and laminin-coated polycarbonate filters. Migration of Raji/CD9h and Raji/CD9f on either substrate was inhibited by the anti-CD9 mAb 50H.19 and by the anti-␤1 integrin mAb AP-138. Migration of Raji/CD9h on laminin was potently inhibited by the anti-VLA-6 integrin mAb GoH3 and by the anti-VLA-4 integrin mAb 44H6, whereas migration of Raji/CD9h on fibronectin was inhibited only by mAb 44H6. Since CD9h-transfected Raji cells adhered to fibronectin as effectively as mock transfectants, expression of CD9 enhanced motility, but not adhesion. CD9-enhanced migration was inhibited by the protein tyrosine kinase inhibitor herbimycin A suggesting that tyrosine phosphorylation played a role in the generation of a motorgenic signal. Raji/CD9h transfectants adherent to fibronectin expressed 6-fold higher levels of phosphotyrosine than Raji. Raji/CD9f transfectants also phosphorylated proteins on tyrosine more effectively than Raji including a protein of 110 kDa which was phosphorylated on the motility-inducing substrates laminin and fibronectin, but not on bovine serum albumin. Our results support a role for CD9 in the amplification of a motorgenic signal in B cells involving ␤1 integrins and the activation of protein tyrosine kinases.

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Section: Cd9 Enhanced Motility and Tyrosine Phosphorylationmentioning

confidence: 99%

Ectopic Expression of Human and Feline CD9 in a Human B Cell Line Confers β1 Integrin-dependent Motility on Fibronectin and Laminin Substrates and Enhanced Tyrosine Phosphorylation

Shaw

Domanska

Mak

et al. 1995

Journal of Biological Chemistry

124

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“…In contrast, decreases in the a2-and a3-or a6-and b4-subunits, or all of them, have been consistently noted in many types of carcinomas. This pattern is exemplified in carcinoma of the breast (15,19,(22)(23)(24), lung (16), colon (14,17,18,25), kidney (20,21), pancreas (26), bladder (27), basal cell carcinoma of the skin (28) and oral squamous cell carcinoma (29). Re-expression of the a2b1 integrin in a poorly differentiated mammary carcinoma resulted in an alteration in phenotype from a fibroblastoid, invasive cell to an epithelioid, less motile and less invasive type of cell (56).…”

Section: European Journal Of Endocrinology (1998) 138mentioning

confidence: 99%

“…The aggressiveness of several malignant tumors correlates with alterations in the expression of one or more integrins. In particular, decreases in the a2-and a3-or the a6-and b4-subunits, or in all of them, have been consistently noted in certain kinds of tumors (14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29).…”

Section: Introductionmentioning

confidence: 99%

Integrins in thyroid tissue: upregulation of alpha2beta1 in anaplastic thyroid carcinoma

Dahlman

Grimelius²,

Wallin³

et al. 1998

European Journal of Endocrinology

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Objective: To evaluate the integrin pattern in the normal thyroid gland and in different pathological disorders including malignant tumors, because the aggressiveness of several malignant tumors correlates with alterations in the expression of one or more integrins. Design: We examined the expression of integrins and E-cadherin immunohistochemically in a large and well-defined sample of normal and pathological human thyroid tissue. Methods: Cryosections of 58 thyroid tissue specimens from normal tissue, thyrotoxicosis, nodular goiter, oxyphilic adenoma, follicular adenoma, follicular carcinoma, papillary carcinoma and anaplastic carcinoma, and three lymph node metastases were investigated immunohistochemically using monoclonal antibodies specifically recognizing the integrin b1-, b4-, a1-, a2-, a3-, a5-and a6-subunits, or E-cadherin. Results: All thyroid epithelial cells expressed integrin b1-and a3-subunits. Immunostaining of the b4-subunit and the a6-subunits was found only in tumors. The staining pattern in the three lymph node metastases from papillary carcinomas did not differ from that in their primaries. Anaplastic carcinomas demonstrated neoexpression of the integrin a2-subunit. E-cadherin was detected in all tissues except anaplastic carcinomas. Conclusions: Neoexpression of a6b4 was seen in most malignant tumors, whereas a2 was exclusively found in anaplastic carcinomas. In the latter, a loss of E-cadherin expression was also seen. These changes in cell adhesion molecule expression strongly suggest an association with the acquisition of proliferative and invasive properties.

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“…Similarly, ITGA6 was found to be overexpressed in breast cancer and contributes toward the resistance to radiation therapy, partially through the activation of PI3K/Akt or MEK/Erk signaling pathways 56 . This α‐subunit may associate with ITGB1 or ITGB4 forming VLA‐6 (α6β1 or α6β4) and act as a laminin receptor 57,58 . Overexpression of ITGAX was associated with aggressive prostate cancer, but we identified only one report where a moderate expression in invasive breast cancer tissue sample was reported 59,60 .…”

Section: Discussionmentioning

confidence: 99%

“…56 This α-subunit may associate with ITGB1 or ITGB4 forming VLA-6 (α6β1 or α6β4) and act as a laminin receptor. 57,58 Overexpression of ITGAX was associated with aggressive prostate cancer, but we identified only one report where a moderate expression in invasive breast cancer tissue sample was reported. 59,60 The siRNA library also contained siRNA against various other integrin-α (ITGA) genes, including ITGA1, ITGA2, ITGA2B, ITGA3, ITGA5, ITGA7, ITGA8, ITGA9, ITGA10, ITGA11, ITGAD, ITGAE, ITGAL, ITGAM, ITGAV, and ITFG2 (integrin-a FG-GAP repeat containing 2), whose silencing did not manifest any effect on migration or cell growth inhibition in this study.…”

Section: Combinational Treatmentmentioning

confidence: 92%

Linoleic‐acid‐substituted polyethylenimine to silence heat shock protein 90B1 (HSP90B1) to inhibit migration of breast cancer cells

Sundaram

Uludağ

2022

The Journal of Gene Medicine

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Introduction Breast cancer continues to be one of the leading causes of death in women, and the lack of treatment options for distant metastasis warrants the need to identify and develop more effective approaches. The aim of this study was to identify and validate targets that are associated with the survival and migration of the breast cancer cells in vitro through RNA interference (RNAi) approach. Methods Linoleic‐acid‐modified polyethylenimine (PEI) polymer was used to screen a short interfering RNA (siRNA) library against numerous cell adhesion and cytoskeleton genes in MDA‐MB‐231 triple‐negative breast cell line, and the functional outcome of silencing was determined by growth and migration inhibition with further target validation studies. Results Heat shock protein 90B1 (HSP90B1) was identified as a crucial gene that is known to be involved in various breast cancer machineries, including uncontrolled proliferation and brain metastasis. The success of this approach was also due to the use of hyaluronic acid (HA) additive in lipopolymer complexes that showed a profound impact in reducing the cell viability (~50%), migration (~40%), and mRNA transcript levels (~80%) with a physiologically relevant siRNA concentration of 60 nM. The use of Dicer‐substrate siRNA proved to be beneficial in target silencing, and a combinational treatment of integrin‐β1 (ITGB1) and HSP90B1 was effective in reducing the migration of the MDA‐MB‐231 and MDA‐MB‐436 breast cancer cells. Conclusion This study demonstrates the potential to identify and silence targets using a lipid‐modified PEI/siRNA system and highlights the importance of HSP90B1 in the growth and migration of breast cancer cells.

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A role of VLA‐6 laminin receptor in invasion of breast carcinoma

Cited by 6 publications

References 26 publications

Ectopic Expression of Human and Feline CD9 in a Human B Cell Line Confers β1 Integrin-dependent Motility on Fibronectin and Laminin Substrates and Enhanced Tyrosine Phosphorylation

Ectopic Expression of Human and Feline CD9 in a Human B Cell Line Confers β1 Integrin-dependent Motility on Fibronectin and Laminin Substrates and Enhanced Tyrosine Phosphorylation

Integrins in thyroid tissue: upregulation of alpha2beta1 in anaplastic thyroid carcinoma

Linoleic‐acid‐substituted polyethylenimine to silence heat shock protein 90B1 (HSP90B1) to inhibit migration of breast cancer cells

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